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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00740: Variant p.Arg75Gln

Coagulation factor IX
Gene: F9
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Variant information Variant position: help 75 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Arginine (R) to Glutamine (Q) at position 75 (R75Q, p.Arg75Gln). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (R) to medium size and polar (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In HEMB; mild. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 75 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 461 The length of the canonical sequence.
Location on the sequence: help FVQGNLERECMEEKCSFEEA R EVFENTERTTEFWKQYVDGD The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         FVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGD

                              FVRGNLERECIEEKCSFEEAREVFENTEKTTEFWKQYVDGD

Chimpanzee                    FVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGD

Mouse                         FVRGNLERECIEERCSFEEAREVFENTEKTTEFWKQYVDGD

Rat                           FVQGNLERECIEERCSFEEAREVFENTEKTTEFWKQYVDGD

Bovine                        FVRGNLERECKEEKCSFEEAREVFENTEKTTEFWKQYVDGD

Cat                           FVQGNLERECMEEKCSFEEAREVFENTEKTTEFWKQYVDGD

Chicken                       LIPGNLERECIEEKCSFEEAREVFENTEKTMEFWKIYIDGD
Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 47 – 461 Coagulation factor IX
Chain 47 – 191 Coagulation factor IXa light chain
Domain 47 – 92 Gla
Binding site 61 – 61 via 4-carboxyglutamate
Binding site 61 – 61 via 4-carboxyglutamate
Binding site 63 – 63 via 4-carboxyglutamate
Binding site 63 – 63 via 4-carboxyglutamate
Binding site 63 – 63 via 4-carboxyglutamate
Binding site 66 – 66 via 4-carboxyglutamate
Binding site 66 – 66 via 4-carboxyglutamate
Binding site 67 – 67 via 4-carboxyglutamate
Binding site 72 – 72 via 4-carboxyglutamate
Binding site 72 – 72 via 4-carboxyglutamate
Binding site 73 – 73 via 4-carboxyglutamate
Binding site 73 – 73 via 4-carboxyglutamate
Binding site 76 – 76 via 4-carboxyglutamate
Binding site 76 – 76 via 4-carboxyglutamate
Binding site 76 – 76 via 4-carboxyglutamate
Binding site 82 – 82 via 4-carboxyglutamate
Binding site 82 – 82 via 4-carboxyglutamate
Binding site 86 – 86 via 4-carboxyglutamate
Binding site 86 – 86 via 4-carboxyglutamate
Binding site 93 – 93
Binding site 94 – 94
Modified residue 61 – 61 4-carboxyglutamate
Modified residue 63 – 63 4-carboxyglutamate
Modified residue 66 – 66 4-carboxyglutamate
Modified residue 67 – 67 4-carboxyglutamate
Modified residue 72 – 72 4-carboxyglutamate
Modified residue 73 – 73 4-carboxyglutamate
Modified residue 76 – 76 4-carboxyglutamate
Modified residue 79 – 79 4-carboxyglutamate
Modified residue 82 – 82 4-carboxyglutamate
Modified residue 86 – 86 4-carboxyglutamate
Glycosylation 85 – 85 O-linked (GalNAc...) threonine
Helix 71 – 75



Literature citations
Functionally important regions of the factor IX gene have a low rate of polymorphism and a high rate of mutation in the dinucleotide CpG.
Koeberl D.D.; Bottema C.D.; Buerstedde J.-M.; Sommer S.S.;
Am. J. Hum. Genet. 45:448-457(1989)
Cited for: VARIANTS HEMB GLN-75; ASP-79; TRP-268; THR-279; SER-306; MET-342; ARG-357 AND ARG-453; VARIANT PHE-7;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.